{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Huang Y"],"funding":["NHLBI NIH HHS","National Heart, Lung, and Blood Institute","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["592-600"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4287833"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["87(1)"],"pubmed_abstract":["Heparan sulfate (HS) 3-O-sulfation determines the binding specificity of HS/heparin for antithrombin III and plays a key role in herpes simplex virus (HSV) infection. However, the low natural abundance of HS 3-O-sulfation poses a serious challenge for functional studies other than the two cases mentioned above. By contrast, multiple distinct isoforms of 3-O-sulfotranserases exist in mammals (up to seven isoenzymes). Here we describe a novel peeling reaction that specifically degrades HS chains with 3-O-sulfated glucosamine at the reducing-end. When HS/heparin is enzymatically depolymerized for compositional analysis, 3-O-sulfated glucosamine at the reducing ends appears to be susceptible to degradation under mildly basic conditions. We propose a 3-O-desulfation initiated peeling reaction m"],"journal":["Analytical chemistry"],"pubmed_title":["Discovery of a heparan sulfate 3-O-sulfation specific peeling reaction."],"pmcid":["PMC4287833"],"funding_grant_id":["P41GM103390","R21 HL131554","R01HL098950","P41 GM103390","P41GM104603","P41 GM104603"],"pubmed_authors":["Zong C","Boons GJ","Huang Y","Lin C","Zaia J","Mao Y"],"additional_accession":[]},"is_claimable":false,"name":"Discovery of a heparan sulfate 3-O-sulfation specific peeling reaction.","description":"Heparan sulfate (HS) 3-O-sulfation determines the binding specificity of HS/heparin for antithrombin III and plays a key role in herpes simplex virus (HSV) infection. However, the low natural abundance of HS 3-O-sulfation poses a serious challenge for functional studies other than the two cases mentioned above. By contrast, multiple distinct isoforms of 3-O-sulfotranserases exist in mammals (up to seven isoenzymes). Here we describe a novel peeling reaction that specifically degrades HS chains with 3-O-sulfated glucosamine at the reducing-end. When HS/heparin is enzymatically depolymerized for compositional analysis, 3-O-sulfated glucosamine at the reducing ends appears to be susceptible to degradation under mildly basic conditions. We propose a 3-O-desulfation initiated peeling reaction m","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Jan","modification":"2025-04-04T14:40:18.286Z","creation":"2019-03-27T01:43:01Z"},"accession":"S-EPMC4287833","cross_references":{"pubmed":["25486437"],"doi":["10.1021/ac503248k"]}}